Gastric proton pump localization. Application of triphosphatase and monophosphatase techniques. | Zendy

J. Anthony Firth | Zendy; G Stranks | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Gastric proton pump localization. Application of triphosphatase and monophosphatase techniques.

Author(s) -

J. Anthony Firth,

G Stranks

Publication year - 1981

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/29.3.6263967

Subject(s) - chemistry , potassium , dephosphorylation , atpase , adenosine triphosphate , biochemistry , phosphatase , phosphate , adenosine triphosphatase , biophysics , lamina propria , enzyme , biology , epithelium , organic chemistry , genetics

Potassium-dependent phosphatase activity can be demonstrated in unfixed frozen sections of mouse stomach using either adenosine triphosphate (ATP) or p-nitrophenyl phosphate (NPP) as substrate. In both cases the potassium-dependent reaction is confined to oxyntic cells, but with ATP, a strong, potassium-independent reaction occurs in the connective tissue of the lamina propria and elsewhere. In the NPP system potassium-independent reaction is very slight, and the oxyntic cell reaction shows responses to inhibitors that differentiate it from Na+, K+-ATPase and that are consistent with its identification with the dephosphorylation step of the proton pump enzyme H+, K+-ATPase, recognized as the active transport component in gastric acid secretion.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research